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PDBsum entry 1b0r
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protein ligands Protein-protein interface(s) links
Signaling protein PDB id
1b0r

 

 

 

 

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Contents
Protein chains
269 a.a. *
100 a.a. *
Ligands
GLY-ILE-LEU
VAL-PHE-THR-CDE
* Residue conservation analysis
PDB id:
1b0r
Name: Signaling protein
Title: Crystal structure of hla-a 0201 Complexed with a peptide with the carboxyl-terminal group substituted by a methyl group
Structure: Protein (hla-a 0201). Chain: a. Fragment: extracellular domains alpha 1,alpha 2 and alpha 3. Engineered: yes. Protein (hla-a 0201). Chain: b. Fragment: beta 2 microglobulin. Engineered: yes. Protein (influenza matrix peptide).
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: extracellular. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Other_details: matrix peptide
Biol. unit: Trimer (from PQS)
Resolution:
2.90Å     R-factor:   0.253     R-free:   0.314
Authors: M.Bouvier,H.Guo,K.J.Smith,D.C.Wiley
Key ref: M.Bouvier et al. (1998). Crystal structures of HLA-A*0201 complexed with antigenic peptides with either the amino- or carboxyl-terminal group substituted by a methyl group. Proteins, 33, 97. PubMed id: 9741848
Date:
12-Nov-98     Release date:   25-Nov-99    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P04439  (1A03_HUMAN) -  HLA class I histocompatibility antigen, A alpha chain from Homo sapiens
Seq:
Struc: 		365 a.a.
269 a.a.*
Protein chain
Pfam   ArchSchema ?
P61769  (B2MG_HUMAN) -  Beta-2-microglobulin from Homo sapiens
Seq:
Struc: 		119 a.a.
100 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 20 residue positions (black crosses)

 

 
Proteins 33:97 (1998)
PubMed id: 9741848  
 
 
Crystal structures of HLA-A*0201 complexed with antigenic peptides with either the amino- or carboxyl-terminal group substituted by a methyl group.
M.Bouvier, H.C.Guo, K.J.Smith, D.C.Wiley.
 
  ABSTRACT  
 
The crystal structures of class I major histocompatibility complex (MHC) molecules complexed with antigenic peptides revealed a network of hydrogen bonds between the charged amino- and carboxyl-termini of the peptides and conserved MHC residues at both ends of the peptide binding site. These interactions were shown to contribute substantially to the stability of class I MHC/peptide complexes by thermal denaturation studies using synthetic peptides in which either the amino- or carboxyl-terminal group is substituted by a methyl group. Here we report crystal structures of HLA-A*0201 complexed with these terminally modified synthetic peptides showing that they adopt the same bound conformation as antigenic peptides. A number of variations in peptide conformation were observed for the terminally modified peptides, including in one case, a large conformational difference in four central peptide residues that is apparently caused by the lattice contact. This is reminiscent of the way binding a T-cell receptor changed the conformation of central residues of an MHC-bound peptide. The structures determined identify which conserved hydrogen bonds are eliminated in terminally substituted peptides and suggest an increased energetic importance of the interactions at the peptide termini for MHC-peptide stability.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19955560 Y.Sun, J.Liu, M.Yang, F.Gao, J.Zhou, Y.Kitamura, B.Gao, P.Tien, Y.Shu, A.Iwamoto, Z.Chen, and G.F.Gao (2010).
Identification and structural definition of H5-specific CTL epitopes restricted by HLA-A*0201 derived from the H5N1 subtype of influenza A viruses.
  J Gen Virol, 91, 919-930.
PDB codes: 3mgo 3mgt
18852655 N.Sasaki, A.Idica, and P.I.Terasaki (2008).
Mimetic human leukocyte antigen epitopes: shown by monoclonal antibodies and extra antibodies produced on transplantation.
  Transplantation, 86, 912-918.  
18159232 Z.Liu, X.Zheng, J.Wang, and E.Wang (2007).
Molecular Analysis of Thymopentin Binding to HLA-DR Molecules.
  PLoS ONE, 2, e1348.  
16451209 Y.S.Heo, S.H.Hwang, O.J.Kwon, S.S.Hur, and H.B.Oh (2006).
Structural aspect of novel HLA-A*02 allele, A*0286, identified by sequence-based typing.
  Tissue Antigens, 67, 84-85.  
  15814707 O.Y.Borbulevych, T.K.Baxter, Z.Yu, N.P.Restifo, and B.M.Baker (2005).
Increased immunogenicity of an anchor-modified tumor-associated antigen is due to the enhanced stability of the peptide/MHC complex: implications for vaccine design.
  J Immunol, 174, 4812-4820.
PDB codes: 1tvb 1tvh
15004033 A.I.Webb, M.A.Dunstone, W.Chen, M.I.Aguilar, Q.Chen, H.Jackson, L.Chang, L.Kjer-Nielsen, T.Beddoe, J.McCluskey, J.Rossjohn, and A.W.Purcell (2004).
Functional and structural characteristics of NY-ESO-1-related HLA A2-restricted epitopes and the design of a novel immunogenic analogue.
  J Biol Chem, 279, 23438-23446.
PDB codes: 1s9w 1s9x 1s9y
15493870 C.A.Wright, P.Kozik, M.Zacharias, and S.Springer (2004).
Tapasin and other chaperones: models of the MHC class I loading complex.
  Biol Chem, 385, 763-778.  
15131131 T.K.Baxter, S.J.Gagnon, R.L.Davis-Harrison, J.C.Beck, A.K.Binz, R.V.Turner, W.E.Biddison, and B.M.Baker (2004).
Strategic mutations in the class I major histocompatibility complex HLA-A2 independently affect both peptide binding and T cell receptor recognition.
  J Biol Chem, 279, 29175-29184.  
12479822 A.Achour, J.Michaëlsson, R.A.Harris, J.Odeberg, P.Grufman, J.K.Sandberg, V.Levitsky, K.Kärre, T.Sandalova, and G.Schneider (2002).
A structural basis for LCMV immune evasion: subversion of H-2D(b) and H-2K(b) presentation of gp33 revealed by comparative crystal structure.Analyses.
  Immunity, 17, 757-768.
PDB codes: 1n59 1n5a
12010576 P.E.Adrian, G.Rajaseger, V.S.Mathura, M.K.Sakharkar, and P.Kangueane (2002).
Types of inter-atomic interactions at the MHC-peptide interface: identifying commonality from accumulated data.
  BMC Struct Biol, 2, 2.  
11557759 J.Yague, A.Marina, J.Vazquez, and J.A.Lopez De Castro (2001).
Major histocompatibility complex class I molecules bind natural peptide ligands lacking the amino-terminal binding residue in vivo.
  J Biol Chem, 276, 43699-43707.  
11536359 O.Schueler-Furman, Y.Altuvia, and H.Margalit (2001).
Examination of possible structural constraints of MHC-binding peptides by assessment of their native structure within their source proteins.
  Proteins, 45, 47-54.  
10859333 J.Yagüe, I.Alvarez, D.Rognan, M.Ramos, J.Vázquez, and J.A.de Castro (2000).
An N-acetylated natural ligand of human histocompatibility leukocyte antigen (HLA)-B39. Classical major histocompatibility complex class I proteins bind peptides with a blocked NH(2) terminus in vivo.
  J Exp Med, 191, 2083-2092.  
10607669 K.Maenaka, and E.Y.Jones (1999).
MHC superfamily structure and the immune system.
  Curr Opin Struct Biol, 9, 745-753.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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